BRENDA - Enzyme Database show
show all sequences of 4.1.99.5

Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase

Zhang, L.; Liang, Y.; Wu, W.; Tan, X.; Lu, X.; Biotechnol. Biofuels 9, 80 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene PMT1231, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain BW25113(DE3) DELTA13
Prochlorococcus marinus
Engineering
Amino acid exchange
Commentary
Organism
I127G
site-directed mutagenesis, increased activity compared to wild-type
Prochlorococcus marinus
I127G/A48G
site-directed mutagenesis, increased activity compared to wild-type
Prochlorococcus marinus
additional information
screening for Prochlorococcus marinus enzyme ADO mutants generated by engineering the active center to accommodate branched-chain isobutyraldehyde, identification of two ADO mutants, I127G and I127G/A48G, which exhibit higher catalytic activity for isobutyraldehyde and 3fold improved propane productivity compared to wild-type, propane biosynthesis generation
Prochlorococcus marinus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus MIT 9313
-
an alkane + formate + H2O + 2 NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Prochlorococcus marinus
Q7V6D4
-
-
Prochlorococcus marinus MIT 9313
Q7V6D4
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747353
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747353
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
isobutyraldehyde + O2 + 2 NADPH + 2 H+
low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G
747353
Prochlorococcus marinus
propane + formate + H2O + 2 NADP+
-
-
-
?
isobutyraldehyde + O2 + 2 NADPH + 2 H+
low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G
747353
Prochlorococcus marinus MIT 9313
propane + formate + H2O + 2 NADP+
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Prochlorococcus marinus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Prochlorococcus marinus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene PMT1231, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain BW25113(DE3) DELTA13
Prochlorococcus marinus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Prochlorococcus marinus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
I127G
site-directed mutagenesis, increased activity compared to wild-type
Prochlorococcus marinus
I127G/A48G
site-directed mutagenesis, increased activity compared to wild-type
Prochlorococcus marinus
additional information
screening for Prochlorococcus marinus enzyme ADO mutants generated by engineering the active center to accommodate branched-chain isobutyraldehyde, identification of two ADO mutants, I127G and I127G/A48G, which exhibit higher catalytic activity for isobutyraldehyde and 3fold improved propane productivity compared to wild-type, propane biosynthesis generation
Prochlorococcus marinus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus
-
an alkane + formate + H2O + 2 NADP+
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
Prochlorococcus marinus MIT 9313
-
an alkane + formate + H2O + 2 NADP+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747353
Prochlorococcus marinus
an alkane + formate + H2O + 2 NADP+
-
-
-
?
a long-chain aldehyde + O2 + 2 NADPH + 2 H+
-
747353
Prochlorococcus marinus MIT 9313
an alkane + formate + H2O + 2 NADP+
-
-
-
?
isobutyraldehyde + O2 + 2 NADPH + 2 H+
low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G
747353
Prochlorococcus marinus
propane + formate + H2O + 2 NADP+
-
-
-
?
isobutyraldehyde + O2 + 2 NADPH + 2 H+
low activity with the wild-type enzyme, but increased activity with enzyme mutants I127G and I127G/A48G
747353
Prochlorococcus marinus MIT 9313
propane + formate + H2O + 2 NADP+
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Prochlorococcus marinus
General Information
General Information
Commentary
Organism
physiological function
enzyme ADO natively catalyzes the conversion of long-chain aldehydes into corresponding alkanes. To convert short-chain isobutyraldehyde into propane efficiently, the substrate specificity of ADO has to be modified for the utilization of the short-chain aldehydes
Prochlorococcus marinus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
enzyme ADO natively catalyzes the conversion of long-chain aldehydes into corresponding alkanes. To convert short-chain isobutyraldehyde into propane efficiently, the substrate specificity of ADO has to be modified for the utilization of the short-chain aldehydes
Prochlorococcus marinus
Other publictions for EC 4.1.99.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
747409
Wang
Identification of residues im ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2, Synechocystis sp. PCC 6803
BMC Biotechnol.
17
31-39
2017
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1
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28
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2
2
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9
9
748564
Patrikainen
Comparison of orthologous cya ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102, Prochlorococcus marinus, Prochlorococcus marinus MIT 9313, Synechococcus sp. RS9917, Synechocystis sp. PCC 6803
Metab. Eng. Commun.
5
9-18
2017
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4
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13
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30
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746976
Park
Crystal structures of aldehyd ...
Limnothrix redekei, Limnothrix redekei KNUA012, Oscillatoria sp. KNUA011
Biochem. Biophys. Res. Commun.
477
395-400
2016
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2
2
2
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4
4
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747351
Bao
Structure-oriented substrate ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2
Biotechnol. Biofuels
9
185
2016
-
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1
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13
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7
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2
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1
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1
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13
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7
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1
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14
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1
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8
1
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2
2
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8
8
747353
Zhang
Microbial synthesis of propan ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
Biotechnol. Biofuels
9
80
2016
-
-
1
-
3
-
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2
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7
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1
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1
1
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747081
Warui
Efficient delivery of long-ch ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
Biochemistry
54
1006-1015
2015
-
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2
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9
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2
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748027
Rajakovich
Rapid reduction of the diferr ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
J. Am. Chem. Soc.
137
11695-11709
2015
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1
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8
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10
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1
1
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748032
Shokri
Conversion of aldehyde to alk ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
J. Am. Chem. Soc.
137
7686-7691
2015
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1
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1
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2
2
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749051
Hayashi
Role of cysteine residues in ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133 / PCC 73102
PLoS ONE
10
e0122217
2015
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1
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8
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1
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1
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7
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10
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1
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8
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1
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10
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1
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5
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3
3
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749212
Jia
Structural insights into the ...
Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC 7942 R2
Protein Cell
6
55-67
2015
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1
1
3
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6
1
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1
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4
4
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726552
Das
Mechanistic insights from reac ...
Nostoc punctiforme
ACS Chem. Biol.
9
570-577
2014
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1
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1
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746597
Buer
Insights into substrate and m ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
ACS Chem. Biol.
9
2584-2593
2014
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2
2
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747074
Waugh
Solvent isotope effects on al ...
Prochlorococcus marinus, Prochlorococcus marinus MIT9313
Biochemistry
53
5537-5543
2014
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1
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3
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6
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1
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726548
Aukema
Cyanobacterial aldehyde deform ...
Prochlorococcus marinus, Prochlorococcus marinus MIT 9313
ACS Catal.
3
2228-2238
2013
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727215
Zhang
Conversion of fatty aldehydes ...
Synechococcus elongatus
Biotechnol. Biofuels
6
86
2013
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727312
Khara
Production of propane and othe ...
Prochlorococcus marinus, Prochlorococcus marinus MIT9313
ChemBioChem
14
1204-1208
2013
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1
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727690
Pandelia
Substrate-triggered addition o ...
Nostoc punctiforme
J. Am. Chem. Soc.
135
15801-15812
2013
1
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1
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727693
Paul
Probing the mechanism of cyano ...
Nostoc punctiforme
J. Am. Chem. Soc.
135
5234-5237
2013
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727001
Li
Evidence for only oxygenative ...
Prochlorococcus marinus
Biochemistry
51
7908-7916
2012
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1
1
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715293
Warui
Detection of formate, rather t ...
Nostoc punctiforme
J. Am. Chem. Soc.
133
3316-3319
2011
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1
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1
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2
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1
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4
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1
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1
1
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1
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726957
Eser
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4
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4
4
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4
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15
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4
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4
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4
4
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713511
Schirmer
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1
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2
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1
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4
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7
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2
1
1
1
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1
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1
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1
1
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2
1
1
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1
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Cheesbrough
Alkane biosynthesis by decarbo ...
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1
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